Tsui, Tung-Yu and Siu, Y. T. and Schlitt, Hans Juergen and Fan, S. T. (2005) Heme oxygenase-1-derived carbon monoxide stimulates adenosine triphosphate generation in human hepatocyte. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 336 (3). pp. 898-902. ISSN 0006-291X,
Full text not available from this repository. (Request a copy)Abstract
Heme oxygenases cleave the pro-oxidant heme molecule into carbon monoxide, ferrous iron, and biliverdin, which is subsequently converted to bilirubin. Increasing the enzymatic activities of heme oxygenase by expression of its inducible isoform, heme oxygenase-1, protects hepatocyte from apoptosis. In the present study, we investigated the mechanisms involving in heme oxygenase-1-mediated cytoprotection. Heme oxygenase-1 could induce the expression of anti-apoptotic protein-Bcl-xL in human hepatocyte. This effect is associated with the activation of p38 MAPK signaling pathway. Carbon monoxide derived from heme oxygenase activities significantly increased adenosine triphosphate levels in hepatocyte that was essential for potentiation of the activation of p38 MAPK signaling. Our demonstration of the importance of the energy status to maximize an anti-apoptotic response provides a new insight into HO-mediated cytoprotection. (c) 2005 Elsevier Inc. All rights reserved.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | NITRIC-OXIDE; ISCHEMIA/REPERFUSION INJURY; GUANYLYL CYCLASE; RAT-LIVER; MITOCHONDRIA; EXPRESSION; PROTECTS; SURVIVAL; SYSTEM; DEATH; adenosine triphosphate; energy metabolism; soluble guanylyl cyclase.; p38 mitogen-activated protein kinase; apoptosis; hepatocyte |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Chirurgie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 26 Apr 2021 05:12 |
| Last Modified: | 26 Apr 2021 05:12 |
| URI: | https://pred.uni-regensburg.de/id/eprint/35510 |
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